Stability-activity tradeoffs constrain the adaptive evolution of RubisCO

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 111; no. 6; pp. 2223 - 2228
• Main Authors: Studer, Romain A., Christin, Pascal-Antoine, Williams, Mark A., Orengo, Christine A.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 11.02.2014; National Acad Sciences
• Subjects: Active sites; Adaptation, Physiological; Amino acids; Angiospermae; Binding sites; Biological adaptation; Biological Evolution; Biological Sciences; Carbon Dioxide - metabolism; convergent evolution; Dimers; Ecological adaptation; Enzyme Stability; Enzymes; Evolution; evolutionary adaptation; Flowering plants; Flowers & plants; Genetic mutation; Models, Molecular; Molecular structure; Mutation; Photosynthesis; Phylogenetics; Phylogeny; Plant Physiological Phenomena; Plants; Positive selection; ribulose-bisphosphate carboxylase; Ribulose-Bisphosphate Carboxylase - chemistry; Ribulose-Bisphosphate Carboxylase - genetics; Ribulose-Bisphosphate Carboxylase - physiology

A well-known case of evolutionary adaptation is that of ribulose-1,5-bisphosphate carboxylase (RubisCO), the enzyme responsible for fixation of CO ₂ during photosynthesis. Although the majority of plants use the ancestral C ₃ photosynthetic pathway, many flowering plants have evolved a derived pathw...